title: High-dimensional NMR spectra for structural studies of biomolecules.
abstract: Recent developments in the acquisition and processing of NMR data sets facilitate the recording of ultra-high-resolution NMR spectra in a reasonable time. The new experiments allow easy resonance assignment for folded and unfolded proteins, as well as the precise determination of spectral parameters, for example, chemical shifts, NOE contacts, coupling constants or cross-correlated relaxation rates. Owing to exceptional resolution of 4D-6D spectroscopy, detailed studies of biomolecules of unprecedented complexity are now possible. Herein, the principles of acquisition and processing methods are presented. The main applications of high-dimensional NMR experiments, including backbone and side-chain resonance assignment in proteins, as well as heteronuclear edited NOE techniques are reviewed.
authors.affiliation: Centre of New Technologies, University of Warsaw, Żwirki i Wigury 93, 02-089 Warsaw (Poland).
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Kazimierczuk
authors.forename: Jan
authors.initials: J
authors.lastname: Stanek
authors.forename: Anna
authors.initials: A
authors.lastname: Zawadzka-Kazimierczuk
authors.forename: Wiktor
authors.initials: W
authors.lastname: Koźmiński
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins
keywords: NMR spectroscopy; bioorganic chemistry; nonuniform sampling; proteins; sparse sampling